Protein Folding and Dynamics─An Overview on the Occasion of Harold Scheraga's 100th Birthday

Gia G. Maisuradze; Gaetano T. Montelione; Shalom Rackovsky; Jeffrey Skolnick

doi:10.1021/acs.jpcb.3c01417

Protein Folding and Dynamics─An Overview on the Occasion of Harold Scheraga's 100th Birthday

Gia G. Maisuradze, Gaetano T. Montelione, Shalom Rackovsky, Jeffrey Skolnick

Icahn School of Medicine at Mount Sinai

Research output: Contribution to journal › Editorial

Original language	English
Pages (from-to)	2879-2880
Number of pages	2
Journal	Journal of Physical Chemistry B
Volume	127
Issue number	13
DOIs	https://doi.org/10.1021/acs.jpcb.3c01417
State	Published - 6 Apr 2023

Access to Document

10.1021/acs.jpcb.3c01417

Cite this

@article{697d759d2cbb480283641511062d1e6c,

title = "Protein Folding and Dynamics─An Overview on the Occasion of Harold Scheraga's 100th Birthday",

author = "Maisuradze, {Gia G.} and Montelione, {Gaetano T.} and Shalom Rackovsky and Jeffrey Skolnick",

note = "Funding Information: This virtual special issue of Journal of Physical Chemistry B is devoted to a survey of protein folding and dynamics, on the occasion of the 100th birthday of Harold A. Scheraga. This dedication is especially apt. Harold{\textquoteright}s career in protein science began in 1946 when he became a postdoctoral fellow in the laboratory of John Edsall, at a time when the most important question in the field was whether proteins are molecules or colloidal aggregates, and the first three-dimensional structure of a protein by X-ray crystallography was 8 years in the future. He left us shortly before his 99th birthday, in August 2020. At the time of his passing his research had been continuously supported by the National Institutes of Health, under the same award, for 64 years, and he had papers in submission, in press, and newly published in leading journals. He presided over the advancement of the field of protein physical chemistry, with magisterial vision and legendary intensity, from the earliest, precrystallographic efforts to determine protein structure hydrodynamically, through pathbreaking experiments on protein folding, to his most recent, cutting-edge work in computational protein chemistry and protein bioinformatics. He carried out seminal work on the elucidation of the blood clotting cascade and on the structure of water. In addition to experimental work, he pioneered the fields of theoretical protein science, protein bioinformatics, computational structure prediction, and protein molecular dynamics. All current efforts in these fields rest on the shoulders of Scheraga{\textquoteright}s early work. He joined the faculty of Cornell University in 1947 as an Instructor in Chemistry, and ended his career there 73 years later as the George W. and Grace L. Todd Professor of Chemistry Emeritus. His bibliography includes almost 1400 publications, he mentored over 400 graduate students and postdoctoral fellows, and he was honored with almost every award the field, and the chemical community at large, had to offer. He was truly a giant of science. ",

year = "2023",

month = apr,

day = "6",

doi = "10.1021/acs.jpcb.3c01417",

language = "English",

volume = "127",

pages = "2879--2880",

journal = "Journal of Physical Chemistry B",

issn = "1520-6106",

publisher = "American Chemical Society",

number = "13",

}

TY - JOUR

T1 - Protein Folding and Dynamics─An Overview on the Occasion of Harold Scheraga's 100th Birthday

AU - Maisuradze, Gia G.

AU - Montelione, Gaetano T.

AU - Rackovsky, Shalom

AU - Skolnick, Jeffrey

N1 - Funding Information: This virtual special issue of Journal of Physical Chemistry B is devoted to a survey of protein folding and dynamics, on the occasion of the 100th birthday of Harold A. Scheraga. This dedication is especially apt. Harold’s career in protein science began in 1946 when he became a postdoctoral fellow in the laboratory of John Edsall, at a time when the most important question in the field was whether proteins are molecules or colloidal aggregates, and the first three-dimensional structure of a protein by X-ray crystallography was 8 years in the future. He left us shortly before his 99th birthday, in August 2020. At the time of his passing his research had been continuously supported by the National Institutes of Health, under the same award, for 64 years, and he had papers in submission, in press, and newly published in leading journals. He presided over the advancement of the field of protein physical chemistry, with magisterial vision and legendary intensity, from the earliest, precrystallographic efforts to determine protein structure hydrodynamically, through pathbreaking experiments on protein folding, to his most recent, cutting-edge work in computational protein chemistry and protein bioinformatics. He carried out seminal work on the elucidation of the blood clotting cascade and on the structure of water. In addition to experimental work, he pioneered the fields of theoretical protein science, protein bioinformatics, computational structure prediction, and protein molecular dynamics. All current efforts in these fields rest on the shoulders of Scheraga’s early work. He joined the faculty of Cornell University in 1947 as an Instructor in Chemistry, and ended his career there 73 years later as the George W. and Grace L. Todd Professor of Chemistry Emeritus. His bibliography includes almost 1400 publications, he mentored over 400 graduate students and postdoctoral fellows, and he was honored with almost every award the field, and the chemical community at large, had to offer. He was truly a giant of science.

PY - 2023/4/6

Y1 - 2023/4/6

UR - http://www.scopus.com/inward/record.url?scp=85151804912&partnerID=8YFLogxK

U2 - 10.1021/acs.jpcb.3c01417

DO - 10.1021/acs.jpcb.3c01417

M3 - Editorial

C2 - 37021400

AN - SCOPUS:85151804912

SN - 1520-6106

VL - 127

SP - 2879

EP - 2880

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

IS - 13

ER -